Modulation of buried ionizable groups in proteins with engineered surface charge.

Abstract

Recent work has shown that proteins can tolerate hydrophobic-to-ionizable-residue mutations. Here, we provide experimental evidence that the essential properties (pK value, protonation state, local dynamics) of buried ionizable groups in proteins can be efficiently modulated through the rational design of the surface charge distribution, thus paving the way for the protein engineering exploitation of charge burial.

DOI: 10.1021/ja909298v

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Cite this paper

@article{Pey2010ModulationOB, title={Modulation of buried ionizable groups in proteins with engineered surface charge.}, author={Angel L Pey and David Rodriguez-Larrea and Jose A Gavira and Bertrand E Garc{\'i}a-Moreno and Jose M. Sanchez-Ruiz}, journal={Journal of the American Chemical Society}, year={2010}, volume={132 4}, pages={1218-9} }